ID I3WJP0_BIFBI Unreviewed; 1578 AA.
AC I3WJP0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Beta-hexosaminidase alpha chain {ECO:0000313|EMBL:AFL05103.1};
DE EC=3.2.1.52 {ECO:0000313|EMBL:AFL05103.1};
GN ORFNames=BBB_1512 {ECO:0000313|EMBL:AFL05103.1};
OS Bifidobacterium bifidum BGN4.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=484020 {ECO:0000313|EMBL:AFL05103.1, ECO:0000313|Proteomes:UP000006173};
RN [1] {ECO:0000313|EMBL:AFL05103.1, ECO:0000313|Proteomes:UP000006173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGN4 {ECO:0000313|EMBL:AFL05103.1,
RC ECO:0000313|Proteomes:UP000006173};
RX PubMed=22887663; DOI=10.1128/JB.00988-12;
RA Yu D.S., Jeong H., Lee D.H., Kwon S.K., Song J.Y., Kim B.K., Park M.S.,
RA Ji G.E., Oh T.K., Kim J.F.;
RT "Complete Genome Sequence of the Probiotic Bacterium Bifidobacterium
RT bifidum Strain BGN4.";
RL J. Bacteriol. 194:4757-4758(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; CP001361; AFL05103.1; -; Genomic_DNA.
DR KEGG; bbf:BBB_1512; -.
DR PATRIC; fig|484020.3.peg.1496; -.
DR HOGENOM; CLU_002275_2_0_11; -.
DR Proteomes; UP000006173; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06564; GH20_DspB_LnbB-like; 1.
DR Gene3D; 2.60.40.3630; -; 2.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR044060; Bacterial_rp_domain.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR022038; Ig-like_bact.
DR PANTHER; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR Pfam; PF07523; Big_3; 2.
DR Pfam; PF00754; F5_F8_type_C; 3.
DR Pfam; PF18998; Flg_new_2; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR PROSITE; PS50022; FA58C_3; 2.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:AFL05103.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AFL05103.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006173};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1552..1573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..123
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 124..282
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 1520..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 698
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 1578 AA; 171597 MW; 8D4F75B907AF7F0A CRC64;
MATTAPEKAV DGDLGTRWGT AQNKAANEWI EVGLGGTKTV KQINIDFERK DADQNITSFK
VELKQGDTYT KVYQKDTRAK QQEIILLDQA QQASAVKVTV LSADGGTMNW VNVGINEISV
YSAPKETVLD TADTNHMLGA TMTASSNETA TLTPDKAIDQ NRTGRNNRWA SGYETPSNIW
LKAEFPRLTA VKDIRIYFFE RDVNPKPTNV QSFDLSYTDS EGTEHTLKSG YAMTASGTGY
VADVVIQLDQ AVNARSLKLS NFAIKSSEYN NVSVAEWEAY SNDQAEPGAT LDSVVSDLES
NHLTIETDTD TLALPTVPDG YTVKFNGADY EQLIAADGTV NHPLVDKTVQ VAYVVTDTAT
GNTKTTSDIP YVVKGTNQQQ EGNNAKPTII PEIAEWHSTS AAKLAASAVT KVVYDDDSLK
AVVDEFVADY KDFTGIKLTA KKGAAEAGAF NFVKTDSTAA IAQLGDEGYT MDIQADRVVA
KSSSVTGNMY AMQTILQMTK QDANGFVIGS MRDYPRFTTR GLLLDVARKP VSLEMMREIT
RTMRYYKMND FQAHLSDNYI FLENYGKGDN EDEAFKAYDA FRLESSLTND KGESPTAEDY
SISKKTFKQF IQDERALGMN VVPEIDVPAH ANSFTKIWPE LMVKGRVSPI NSNRPLIDHL
DVSKPETIAK IKEIFDDYTK GDDPTFDSDT TVHIGADEFL YNYTAYRKFI NEIVPYIKDT
NTVRMWGGLT WINDHKTEIT KDAIENVEMN LWSKDWADGL QMYNMGYKLI NTIDDYGYMV
PNGSYGRANA YGDLLNISRV FDSFEPNKVR SSGGYQAVPS GDDQMLGAAF AIWSDNIDKS
ASGLTESDLY WRFFDAMPFY AEKTWAATGK EKGTAAKLTA LAAKQGTGPR TNPYYQATSK
NSVYESYDFN DGLADASGNG RDLTIGDGSK AAVKDQSLKL AGGSSYATSK LDKLGNGNEL
TFDVTLQQAA KPGDILFEAD APYGPHDIRV MENGKLGFTR ELYNYYFDYE LPVGKTVTVT
IKVDRQTTKL YVDGEFVSDA TGKYIDKGIE KKTGITAATF ALPLQRIGSK TSAINGVIDN
VIVKKSEAET DQYNKSCWTG TTNSETRYND TEGLLRYAFD NNPSTIWHSN WKGATDKLTG
SNSFYAEIDM CQKYTINQFS FTPRTSQDSG QVTKADLYVK ANANDEWKQV ATDQVFEASR
AKKTFMFDEQ EVRYVKFVAK SSNDGWVAVS EFGVANKPSS TVRVFVAADP AEGGTVSVAA
EGETGTDTAV DVASGASVTA KAVAADGYRF SGWFTTASET AVSTDATYTF AADGNTALTA
KFTKDSTPDP DPKPTISSIA VTKPTVTDYK VGDTFDATGL AVTATMSDGS TKTLTAGEYT
LAATQDGAAV ALDKAFAKAG TVTVTVTANG KTATFDVTVT AKNPDPEPAT LKSIKVTSKP
DKTTYTVDET FAKTGLAVTG TWSDGKTALL KDSEYKLSAV DADGKTVDLT KPFTAAGDIT
VTVTSGKFTD SFTITVKAKT VTPTPGDNKP GENKPGADKP KPNTPDEVAK TGASVTAVVF
SALLLLSAGY LLVRKRRI
//
